ID   Q9QWI0_RAT              Unreviewed;       440 AA.
AC   Q9QWI0;
DT   01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2000, sequence version 1.
DT   02-SEP-2026, entry version 150.
DE   SubName: Full=Peroxisome proliferator activated receptor delta {ECO:0000313|EMBL:AAC65985.1};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116 {ECO:0000313|EMBL:AAC65985.1};
RN   [1] {ECO:0000313|EMBL:AAC65985.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Wistar-Kyoto {ECO:0000313|EMBL:AAC65985.1};
RX   PubMed=10559001;
RA   Adams L.D., Lemire J.M., Schwartz S.M.;
RT   "A systematic analysis of 40 random genes in cultured vascular smooth
RT   muscle subtypes reveals a heterogeneity of gene expression and identifies
RT   the tight junction gene zonula occludens 2 as a marker of epithelioid 'pup'
RT   smooth muscle cells and a participant in carotid neointimal formation.";
RL   Arterioscler. Thromb. Vasc. Biol. 19:2600-2608(1999).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|PROSITE-ProRule:PRU00407, ECO:0000256|RuleBase:RU004334}.
CC   -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR1
CC       subfamily. {ECO:0000256|ARBA:ARBA00008092}.
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DR   EMBL; U75918; AAC65985.1; -; mRNA.
DR   AlphaFoldDB; Q9QWI0; -.
DR   UCSC; RGD:3370; rat.
DR   PhylomeDB; Q9QWI0; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004879; F:nuclear receptor activity; IEA:InterPro.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0001223; F:transcription coactivator binding; IEA:UniProtKB-ARBA.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-ARBA.
DR   GO; GO:0010614; P:negative regulation of cardiac muscle hypertrophy; IEA:UniProtKB-ARBA.
DR   GO; GO:0030308; P:negative regulation of cell growth; IEA:UniProtKB-ARBA.
DR   GO; GO:0006950; P:response to stress; IEA:UniProtKB-ARBA.
DR   CDD; cd06965; NR_DBD_Ppar; 1.
DR   CDD; cd06932; NR_LBD_PPAR; 1.
DR   FunFam; 1.10.565.10:FF:000013; Peroxisome proliferator-activated receptor delta; 1.
DR   FunFam; 3.30.50.10:FF:000010; Peroxisome proliferator-activated receptor gamma; 1.
DR   Gene3D; 3.30.50.10; Erythroid Transcription Factor GATA-1, subunit A; 1.
DR   Gene3D; 1.10.565.10; Retinoid X Receptor; 1.
DR   InterPro; IPR003074; 1Cnucl_rcpt.
DR   InterPro; IPR003075; 1Cnucl_rcpt_B.
DR   InterPro; IPR035500; NHR-like_dom_sf.
DR   InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
DR   InterPro; IPR050234; Nuclear_hormone_rcpt_NR1.
DR   InterPro; IPR001723; Nuclear_hrmn_rcpt.
DR   InterPro; IPR001628; Znf_hrmn_rcpt.
DR   InterPro; IPR013088; Znf_NHR/GATA.
DR   PANTHER; PTHR24082; NUCLEAR HORMONE RECEPTOR; 1.
DR   PANTHER; PTHR24082:SF15; PEROXISOME PROLIFERATOR-ACTIVATED RECEPTOR DELTA; 1.
DR   Pfam; PF00104; Hormone_recep; 1.
DR   Pfam; PF00105; zf-C4; 1.
DR   PRINTS; PR01288; PROXISOMEPAR.
DR   PRINTS; PR01290; PROXISOMPABR.
DR   PRINTS; PR00398; STRDHORMONER.
DR   PRINTS; PR00047; STROIDFINGER.
DR   SMART; SM00430; HOLI; 1.
DR   SMART; SM00399; ZnF_C4; 1.
DR   SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR   SUPFAM; SSF48508; Nuclear receptor ligand-binding domain; 1.
DR   PROSITE; PS51843; NR_LBD; 1.
DR   PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
DR   PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
PE   2: Evidence at transcript level;
KW   Activator {ECO:0000256|ARBA:ARBA00023159};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PROSITE-
KW   ProRule:PRU00407};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU004334};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW   ProRule:PRU00407};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|PROSITE-
KW   ProRule:PRU01189};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|PROSITE-
KW   ProRule:PRU00407};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW   ECO:0000256|PROSITE-ProRule:PRU00407};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004334};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00407}.
FT   DOMAIN          70..144
FT                   /note="Nuclear receptor"
FT                   /evidence="ECO:0000259|PROSITE:PS51030"
FT   DOMAIN          210..438
FT                   /note="NR LBD"
FT                   /evidence="ECO:0000259|PROSITE:PS51843"
FT   DNA_BIND        70..144
FT                   /note="Nuclear receptor"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00407"
FT   REGION          1..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          427..438
FT                   /note="AF-2"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01189"
FT   COMPBIAS        36..53
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   440 AA;  49719 MW;  7F050F795586A13C CRC64;
     MEQPQEETPE AREEEKEEVA TGDGAPELNG GPEHTLPSSS CTDLSQNSSP SSLLDQLQMG
     CDGASGGSLN MECRVCGDKA SGFHYGVHAC EGCKGFFRRT IRMKLKYEKC DRICKIQKKN
     RNKCQYCRFQ KCLALGMSHN AIRFGRMPEA EKRKLVAGLT ASEGCQQNPQ LADLKAFSKH
     IYNAYLKNFN MTKKKARSIL TGKSSHNAPF IIHDIETLWQ AEKGLVWKQL VNGPRPYNEI
     SVHVFYRCQS TTVDTVRELT EFAKNIPNFS SLFLNDQVTL LKYGVHQAIF AMLASIVNKD
     GLLVANGSGF VTHEFLRSIR KPFSDIIEPK FEFAVKFNAL ELDDSDLALF IAAIILCGDR
     PGLMNVPQVE AIQDTILQAL EFHLQVNHPD SQYLFPKLLQ KMADLRQLVT EHAQMMQWLK
     KTESETLLHP LLQEIYKDMY
//